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The protein encoded by MID1 is a member of the tripartite motif (TRIM) family, also known as the 'RING-B box-coiled coil' (RBCC) subgroup of RING finger proteins. Additionally we are shipping MID1 Antibodies (58) and MID1 Proteins (9) and many more products for this protein.
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identified four miRNAs, miR (show MLXIP ELISA Kits)-19, miR (show MLXIP ELISA Kits)-340, miR (show MLXIP ELISA Kits)-374 and miR (show MLXIP ELISA Kits)-542 that bind to the 3'-UTR (show UTS2R ELISA Kits) of the MID1 mRNA. These miRNAs not only regulate MID1 expression but also mTOR (show FRAP1 ELISA Kits) signaling and translation of disease associated mRNAs and could therefore serve as potential drugs for future therapy development
Our data reveal a novel role for MID1 and for atypical ubiquitination in balancing BRAF35 presence, and likely its activity, within nuclear and cytoplasmic compartments
P151L MID1 mutation is associated with X-linked Opitz Syndrome.
the coiled-coil and COS domain (CC-COS) bind to microtubules, demonstrating for the first time that MID1 can directly associate with the microtubules
Osx is upregulated in patients with Ossification of the posterior longitudinal ligament.
A130T/V mutations within the MID1 zinc-binding Bbox1 (show BBOX1 ELISA Kits) domain affects protein folding.
MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 (show BBOX1 ELISA Kits) domain disrupt polyubiquitination of alpha4 but not of PP2Ac in X-linked Opitz syndrome.
TRAIL regulates MID1 and TSLP (show TSLP ELISA Kits), inflammation, fibrosis, smooth muscle hypertrophy, and expression of inflammatory effector chemokines and cytokines in experimental eosinophilic esophagitis.
These studies provide insight into the mechanism by which mutations observed in X-linked Opitz G syndrome affect the structure and function of the MID1 Bbox1 (show BBOX1 ELISA Kits) domain
A familial c.1102C>T (p.R368X) mutation in the MID1 gene, is reported.
we show that MID1 controls exocytosis of lytic granules and cytotoxicity in murine cytotoxic lymphocytes
X-linked microtubule-associated protein (show SPAG5 ELISA Kits), Mid1, regulates axon development.
MID1 inhibition also limited rhinovirus-induced exacerbation of allergic airway disease
Thus, lack of Mid1 causes a misspecification of the midbrain/cerebellar boundary that results in an abnormal development of the most anterior cerebellar lobes.
Analysis of Mid1, Hccs (show HCCS ELISA Kits), Arhgap6, and Msl3l1 in X-linked polydactyly (Xpl) and Patchy-fur (Paf (show PAF ELISA Kits)) mutant mice
SHH (show SHH ELISA Kits)-dependent E-ligase Midline1 regulates ubiquitin-mediated proteasomal degradation of Pax6 (show PAX6 ELISA Kits) during visual system development.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also known as the 'RING-B box-coiled coil' (RBCC) subgroup of RING finger proteins. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein forms homodimers which associate with microtubules in the cytoplasm. The protein is likely involved in the formation of multiprotein structures acting as anchor points to microtubules. Mutations in this gene have been associated with the X-linked form of Opitz syndrome, which is characterized by midline abnormalities such as cleft lip, laryngeal cleft, heart defects, hypospadias, and agenesis of the corpus callosum. This gene was also the first example of a gene subject to X inactivation in human while escaping it in mouse. Multiple different transcript variants are generated by alternate splicing\; however, the full-length nature of some of the variants has not been determined.
RING finger protein 59
, midline 1 RING finger protein
, putative transcription factor XPRF
, tripartite motif protein TRIM18
, tripartite motif-containing protein 18
, zinc finger on X and Y, mouse, homolog of
, Finger on X and Y (in rat only on X)
, E3 ubiquitin-protein ligase Midline-1
, midline 1 (Opitz/BBB syndrome)